Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Protein interaction network of the mammalian Hippo pathway reveals mechanisms of kinase-phosphatase interactions.
A proteome-scale map of the human interactome network.
LRCH1 interferes with DOCK8-Cdc42-induced T cell migration and ameliorates experimental autoimmune encephalomyelitis.
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LRCH1 competes with Cdc42 for DOCK8 binding and restrains T-cell migration.
"Using two screening systems, we found that LRCH1 competes with Cdc42 for interaction with DOCK8 and restrains T cell migration."
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LRCH1 binds the catalytic DHR-2 domain of DOCK8 and restricts its guanyl-nucleotide exchange activity.
"Next, we identified that LRCH1 competes with Cdc42 for binding to the catalytic DHR-2 domain of DOCK8 and restricts the GEF activity of DOCK8."
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Chemokine stimulation promotes PKC-alpha-dependent DOCK8 release from LRCH1 and DOCK8 movement to the leading edge.
"In response to chemokine stimulation, PKCα phosphorylates DOCK8 at its three serine sites, promoting DOCK8 separation from LRCH1 and translocation to the leading edge to guide T cell migration."
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The downstream autoimmune phenotype was established in mouse EAE models and should not be generalized as direct human disease mechanism.
"Importantly, Dock8 mutant mice or Lrch1 transgenic mice were protected from MOG (35-55) peptide-induced experimental autoimmune encephalomyelitis (EAE), whereas Lrch1-deficient mice displayed a more severe phenotype."
The MYO6 interactome reveals adaptor complexes coordinating early endosome and cytoskeletal dynamics.
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LRCH1 co-immunoprecipitates DOCK7 but was not observed to interact with MYO6.
"Although other LRCH family members such as LRCH1 were identified in the MYO6 and DOCK7 BioID data sets, no interaction between LRCH1 and MYO6 was observed, although LRCH1 did co‐immunoprecipitate DOCK7"
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DOCK7 proximity labeling recovered LRCH1, LRCH3, and LRCH4, but the paper's mapped MYO6-linker and cytoskeletal mechanism concerns LRCH3 rather than LRCH1.
"BirA*‐DOCK7 labelling identified only three high‐confidence interactions, all of which were LRCH family proteins (LRCH1, LRCH3 and LRCH4)"
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Multimodal cell maps as a foundation for structural and functional genomics.
LRCH1 deficiency enhances LAT signalosome formation and CD8(+) T cell responses against tumors and pathogens.
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LRCH1 binds LAT, reduces LAT phosphorylation and GRB2 association, and promotes LAT endocytosis in the study's T-cell signaling system.
"Here we have demonstrated that LRCH1 (leucine-rich repeats and calponin homology domain containing 1) directly binds LAT, reduces LAT phosphorylation and interaction with GRB2, and also promotes the endocytosis of LAT."
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LRCH1 knockout increased migration and proliferation of human glypican-3 CAR T cells in vitro; this is an engineered-cell context.
"Furthermore, knockout of LRCH1 in human chimeric antigen receptor (CAR) T cells that recognize the liver tumor-associated antigen glypican-3 could improve CAR T cell migration and proliferation in vitro."
LRCH1 suppresses migration of CD4(+) T cells and refers to disease activity in ulcerative colitis.
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Manipulating LRCH1 in human peripheral CD4-positive T cells altered CXCL12-directed migration without altering T-cell differentiation or the assayed cytokines.
"Up or down regulation of LRCH1 did not affect the differentiation of CD4+ T cells, and the related cytokines expression. Moreover, LRCH1 inhibited migratory capacity of CD4+ T cells toward CXCL12 by PKCα."
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LRCH1 expression was lower in active ulcerative-colitis mucosa and PBMCs and inversely associated with disease activity.
"LRCH1 expression was highly decreased in colonic mucosa and PBMCs from patients with A-UC, and negatively correlated with disease activity."
Inhibition of leucine-rich repeats and calponin homology domain containing 1 accelerates microglia-mediated neuroinflammation in a rat traumatic spinal cord injury model.
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LRCH1 knockdown enhanced inflammatory cytokine production and p38/ERK signaling in primed rat microglia.
"LRCH1 knockdown increased the production of pro-inflammatory cytokines such as IL-1β, TNF-α, and IL-6 after in vitro priming with lipopolysaccharide and adenosine triphosphate."
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The study was explicitly performed in primary microglia and a rat SCI model.
"To elucidate the significance of LRCH1 to microglial functions, we applied lentivirus-induced LRCH1 knockdown in primary microglia culture and tested the role of LRCH1 in microglia-mediated inflammatory reaction both in vitro and in a rat SCI model."
Leucine rich repeats and calponin homology domain containing 1 inhibits NK-92 cell cytotoxicity through attenuating Src signaling.
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LRCH1 knockout increased NK-92 cytotoxicity and activation of Src and Lck after tumor-cell contact.
"Further experiments revealed that LRCH1 knockout enhanced the activation of Src and Lck kinase which are important for natural killer cell cytotoxicity."
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LRCH1 knockout also increased IFN-gamma and TNF-alpha production in primary human natural killer cells.
"Importantly, human primary natural killer cells exhibited a similar increase in the production of IFN-γ and TNF-α when LRCH1 was knocked out."
LRCH proteins: a novel family of cytoskeletal regulators.
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The sole Drosophila LRCH protein stabilizes the cell cortex during division, but this family-level result cannot be assigned specifically to human LRCH1.
"Taking advantage of the existence of a single LRCH gene in flies, dLRCH, we explored its function in cultured cells, and show that dLRCH act to stabilize the cell cortex during cell division."
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Human LRCH1-4 share the combined LRR and calponin-homology architecture.
"In human, only four highly-related proteins (hLRCH1-4) simultaneously harbor these two motifs."